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Nucleic Acids Research, 1983, Vol. 11, No. 21 7397-7407
© 1983

MOLECULAR BIOLOGY

Initiation of phage {pi}29 DNA replication by the terminal protein modified at the carboxyl end

Rafael P. Mellado and Margarita Salas

Centro de Biologia Molecular (CSIC-UAM), Facultad de Ciencias, Universidad Aut6noma Canto Blanco, Madrid-34, Spain

Received August 2, 1983. Revised October 12, 1983. Accepted October 12, 1983.

A mutant at the carboxyl end of the terminal protein, p3, of phage {pi}29 DNA has been constructed by inserting an oligonucleo-tide containing the stop translation codon TGA in the three possible reading frames, immediately downstream of a {pi}29 DNA fragment coding for all but the last five amino acids of protein p3. The activity in the formation of the p3-dAMP initiation complex in vitro of this mutant as well as another one previously isolated, also mutated at the carboxyl end, have been tested. The results obtained suggest that an intact carboxyl end in the {pi}29 terminal protein is essential for its normal primer function in DNA replication.


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